Hemolysin of Propionibacterium avidum.

Thiol-activated extracellular hemolysin produced by a strain of Propionibacterium avidum was partially purified and several properties were examined. The hemolysin was heat labile and inactivated by proteases and deoxyribonuclease. Hemolysin adsorbed to erythrocytes at 0 degrees C. Cu++ at 1 mM inhibited hemolysis partially. Lecithin prevented the activity completely. The hemolytic spectrum was relatively wide and the activity was high with rabbit, dog, horse, and pig erythrocytes.